[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Brain, and Testis; DOI=10.1006/bbrc.1994.1150; PubMed=8117261 [NCBI, ExPASy, EBI, Israel, Japan] Tomoda T., Kudoh T., Noma T., Nakazawa A., Muramatsu M.-A., Arai K.; "Molecular cloning of a mouse counterpart for human TGF-beta type I receptor."; Biochem. Biophys. Res. Commun. 198:1054-1062(1994).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). TISSUE=Brain; DOI=10.1006/bbrc.1994.1151; PubMed=8117262 [NCBI, ExPASy, EBI, Israel, Japan] Suzuki A., Shioda N., Maeda T., Tada M., Ueno N.; "A mouse TGF-beta type I receptor that requires type II receptor for ligand binding."; Biochem. Biophys. Res. Commun. 198:1063-1069(1994).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). STRAIN=C57BL/6; TISSUE=Brain; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

Comments

FUNCTION: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for TGF-beta.
CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.
COFACTOR: Magnesium or manganese (By similarity).
SUBUNIT: Interacts with CD109. The unphosphorylated protein interacts with FKBP1A and is stabilized the inactive conformation. Phosphorylation of the GS region abrogates FKBP1A binding. Interacts with SMAD2 when phosphorylated on several residues in the GS region (By similarity).
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein (By similarity).

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	Q64729-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	Q64729-2
Note: May be due to a competing donnor splice site.
Features which should be applied to build the isoform sequence: VSP_021593.

PTM: Phosphorylated at basal levels in the absence of ligand binding. Activated by multiple phosphorylation, mainly in the GS region (By similarity).
SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.
SIMILARITY: Contains 1 GS domain.
SIMILARITY: Contains 1 protein kinase domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D28526; BAA05878.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D25540; BAA05023.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC063260; AAH63260.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JC2061; JC2061.
JC2062; JC2062.

RefSeq

NP_033396.1; -.

UniGene

Mm.197552

3D structure databases

HSSP

P36897; 1IAS. [HSSP ENTRY / PDB]

Q64729; 201-503.

PTM databases

Q64729; -.

Organism-specific databases

MGI

MGI:98728; Tgfbr1.

GeneLynx

Tgfbr1; Mus musculus.

Gene expression databases

ArrayExpress

Q64729; -.

CleanEx

MM_TGFBR1; -.

GermOnline

ENSMUSG00000007613; Mus musculus.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from MGI).
GO:0005024;	Molecular function: transforming growth factor beta receptor activity (inferred from direct assay from MGI).
GO:0009952;	Biological process: anterior/posterior pattern formation (inferred from genetic interaction from MGI).
GO:0048844;	Biological process: artery morphogenesis (inferred from mutant phenotype from MGI).
GO:0030199;	Biological process: collagen fibril organization (inferred from mutant phenotype from MGI).
GO:0048701;	Biological process: embryonic cranial skeleton morphogenesis (inferred from mutant phenotype from MGI).
GO:0008354;	Biological process: germ cell migration (inferred from mutant phenotype from MGI).
GO:0007507;	Biological process: heart development (inferred from mutant phenotype from MGI).
GO:0001701;	Biological process: in utero embryonic development (inferred from mutant phenotype from MGI).
GO:0006917;	Biological process: induction of apoptosis (inferred from mutant phenotype from MGI).
GO:0001822;	Biological process: kidney development (inferred from genetic interaction from MGI).
GO:0043066;	Biological process: negative regulation of apoptosis (inferred from mutant phenotype from MGI).
GO:0048663;	Biological process: neuron fate commitment (inferred from mutant phenotype from MGI).
GO:0060021;	Biological process: palate development (inferred from mutant phenotype from MGI).
GO:0060017;	Biological process: parathyroid gland development (inferred from mutant phenotype from MGI).
GO:0060037;	Biological process: pharyngeal system development (inferred from mutant phenotype from MGI).
GO:0051491;	Biological process: positive regulation of filopodium formation (inferred from mutant phenotype from MGI).
GO:0009791;	Biological process: post-embryonic development (inferred from mutant phenotype from MGI).
GO:0010468;	Biological process: regulation of gene expression (inferred from mutant phenotype from MGI).
GO:0048538;	Biological process: thymus development (inferred from mutant phenotype from MGI).
GO:0007179;	Biological process: transforming growth factor beta receptor signaling pathway (inferred from direct assay from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR000333; Activin_II_recpt.
IPR000472; Activin_rcpt.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR008271; Ser_thr_pkin_AS.
IPR003605; TGF_beta_rcpt_GS.
Graphical view of domain structure.

Pfam

PF01064; Activin_recp; 1.
PF08515; TGF_beta_GS; 1.
Pfam graphical view of domain structure.

PRINTS

PR00653; ACTIVIN2R.

ProDom

PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00467; GS; 1.
SMART graphical view of domain structure.

PROSITE

PS51256; GS; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q64729.

Genome annotation databases

Ensembl

ENSMUSG00000007613; Mus musculus. [Contig view]

GeneID

21812; -.

KEGG

mmu:21812; -.

Phylogenomic databases

HOGENOM

Q64729; -.

HOVERGEN

Q64729; -.

Other

SOURCE

Tgfbr1; Mus musculus.

ProtoNet

Q64729.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; ATP-binding; Glycoprotein; Kinase; Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Receptor; Serine/threonine-protein kinase; Signal; Transferase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 22`	`22`	`Potential.`
`CHAIN`	`23 503`	`481`	`TGF-beta receptor type-1.`	`PRO_0000024424`
`TOPO_DOM`	`23 125`	`103`	`Extracellular (Potential).`
`TRANSMEM`	`126 148`	`23`	`Potential.`
`TOPO_DOM`	`149 503`	`355`	`Cytoplasmic (Potential).`
`DOMAIN`	`175 204`	`30`	`GS.`
`DOMAIN`	`205 495`	`291`	`Protein kinase.`
`NP_BIND`	`211 219`	`9`	`ATP (By similarity).`
`ACT_SITE`	`333 333`		`Proton acceptor (By similarity).`
`BINDING`	`232 232`		`ATP (By similarity).`
`MOD_RES`	`185 185`		`Phosphothreonine (By similarity).`
`MOD_RES`	`186 186`		`Phosphothreonine (By similarity).`
`MOD_RES`	`187 187`		`Phosphoserine (By similarity).`
`MOD_RES`	`189 189`		`Phosphoserine (By similarity).`
`MOD_RES`	`191 191`		`Phosphoserine (By similarity).`
`CARBOHYD`	`41 41`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`32 50`		`By similarity.`
`DISULFID`	`34 37`		`By similarity.`
`DISULFID`	`44 67`		`By similarity.`
`DISULFID`	`82 96`		`By similarity.`
`DISULFID`	`97 102`		`By similarity.`
`VAR_SEQ`	`111 114`		`Missing (in isoform 2).`	`VSP_021593`

Sequence information

Length: 503 AA [This is the length of the unprocessed precursor]

Molecular weight: 56179 Da [This is the MW of the unprocessed precursor]

CRC64: BB8BB6D2261793AF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEAAAAAPRR PQLLIVLVAA ATLLPGAKAL QCFCHLCTKD NFTCETDGLC FVSVTETTDK 

        70         80         90        100        110        120 
VIHNSMCIAE IDLIPRDRPF VCAPSSKTGA VTTTYCCNQD HCNKIELPTT GPFSEKQSAG 

       130        140        150        160        170        180 
LGPVELAAVI AGPVCFVCIA LMLMVYICHN RTVIHHRVPN EEDPSLDRPF ISEGTTLKDL 

       190        200        210        220        230        240 
IYDMTTSGSG SGLPLLVQRT IARTIVLQES IGKGRFGEVW RGKWRGEEVA VKIFSSREER 

       250        260        270        280        290        300 
SWFREAEIYQ TVMLRHENIL GFIAADNKDN GTWTQLWLVS DYHEHGSLFD YLNRYTVTVE 

       310        320        330        340        350        360 
GMIKLALSTA SGLAHLHMEI VGTQGKPAIA HRDLKSKNIL VKKNGTCCIA DLGLAVRHDS 

       370        380        390        400        410        420 
ATDTIDIAPN HRVGTKRYMA PEVLDDSINM KHFESFKRAD IYAMGLVFWE IARRCSIGGI 

       430        440        450        460        470        480 
HEDYQLPYYD LVPSDPSVEE MRKVVCEQKL RPNIPNRWQS CEALRVMAKI MRECWYANGA 

       490        500 
ARLTALRIKK TLSQLSQQEG IKM

Q64729 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools